M L Champigny1. 1. , 11 rue du Docteur Roux, 92330, Sceaux, France.
Abstract
Concomitant assimilation of C and N in illuminated leaves requires the regulated partitioning of reductant and photosynthate to sustain the demands of amino acid and carbohydrate biosynthesis. The short-term responses of photosynthesis and photosynthate partitioning to N enrichment in wheat (Triticum aestivum, L.) and maize (Zea mays L.) leaves were studied in order to understand the regulatory strategy employed in higher plants. Transgenic tobacco plants (Tobacco plumbaginifolia) over-expressing NR or with poor NR expression were used to compare plants differing in their capacities for NO3 (-) assimilation. Similar regulatory responses to NO3 (-) were observed in leaves having C4- and C3-type photosynthesis. It was shown that the extra- C needed in the short-term to sustain amino acid synthesis was not provided by an increase in photosynthetic CO2 fixation but rather by a rapid shift in the partitioning of photosynthetic C to amino acid at the expense of sucrose biosynthesis. The modulation of three enzymes was shown to be important in this C and N interaction, namely PEPCase (EC 4.1.1.31), SPS (EC 2.4.1.14) and NADH/NR (EC 1.6.6.1). The first two enzymes were shown to share the common feature of regulatory post-transcriptional NO3 (-)-dependent phosphorylation of their proteins on a seryl-residue. While PEPCase is activated, SPS activity is decreased. In contrast the NR phosphorylation state is unchanged and all N-dependent control of NR activity is regulated at the protein level. A number of arguments support the hypothesis that Gln, the primary product of NO3 (-) assimilation, is the metabolite effector for short-term modulation of PEPCase, and SPS in response to N enrichment. Since a major effect of NO3 (-) on the PEPCase-protein kinase activity in concentrated wheat leaf extracts was demonstrated, the hypothesis is put forward that protein phosphorylation is the primary event allowing the short-term adaptation of leaf C metabolism to changes in N supply.
Concomitant assimilation of C and N in illuminated leaves requires the regulated partitioning of reductant and photosynthate to sustain the demands of amino acid and carbohydrate biosynthesis. The short-term responses of photosynthesis and photosynthate partitioning to N enrichment inn class="Species">wheat (Triticum aestivum, L.) and maize (Zea mays L.) leaves were studied in order to understand the regulatory strategy employed in higher plants. Transgenic tobacco plants (Tobacco plumbaginifolia) over-expressing NR or with poor NR expression were used to compare plants differing in their capacities for NO3 (-) assimilation. Similar regulatory responses to NO3 (-) were observed in leaves having C4- and C3-type photosynthesis. It was shown that the extra- C needed in the short-term to sustain amino acid synthesis was not provided by an increase in photosynthetic CO2 fixation but rather by a rapid shift in the partitioning of photosynthetic C to amino acid at the expense of sucrose biosynthesis. The modulation of three enzymes was shown to be important in this C and N interaction, namely PEPCase (EC 4.1.1.31), SPS (EC 2.4.1.14) and NADH/NR (EC 1.6.6.1). The first two enzymes were shown to share the common feature of regulatory post-transcriptional NO3 (-)-dependent phosphorylation of their proteins on a seryl-residue. While PEPCase is activated, SPS activity is decreased. In contrast the NR phosphorylation state is unchanged and all N-dependent control of NR activity is regulated at the protein level. A number of arguments support the hypothesis that Gln, the primary product of NO3 (-) assimilation, is the metabolite effector for short-term modulation of PEPCase, and SPS in response to N enrichment. Since a major effect of NO3 (-) on the PEPCase-protein kinase activity in concentrated wheat leaf extracts was demonstrated, the hypothesis is put forward that protein phosphorylation is the primary event allowing the short-term adaptation of leaf C metabolism to changes in N supply.
Authors: C. H. Foyer; J. C. Lescure; C. Lefebvre; J. F. Morot-Gaudry; M. Vincentz; H. Vaucheret Journal: Plant Physiol Date: 1994-01 Impact factor: 8.340